4NG7
Crystal structure of a TRAP periplasmic solute binding protein from Citrobacter koseri (CKO_04899), Target EFI-510094, apo, open structure
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 31-ID |
Synchrotron site | APS |
Beamline | 31-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-08-12 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 0.9793 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 93.503, 93.503, 140.175 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 40.488 - 2.300 |
R-factor | 0.2087 |
Rwork | 0.206 |
R-free | 0.25450 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4n8y |
RMSD bond length | 0.008 |
RMSD bond angle | 1.129 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.20) |
Phasing software | PHENIX |
Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 80.976 | 40.488 | 2.420 |
High resolution limit [Å] | 2.300 | 7.270 | 2.300 |
Rmerge | 0.140 | 0.059 | 0.948 |
Total number of observations | 7008 | 34063 | |
Number of reflections | 16734 | ||
<I/σ(I)> | 13.9 | 9.3 | 0.8 |
Completeness [%] | 99.9 | 97.8 | 99.9 |
Redundancy | 14 | 11.5 | 14.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | 37.4 mg/mL protein in 10 mM HEPES, pH 7.5, 5 mM DTT, 1 mM D-arabinoate, reservoir: 0.1 M Bis-Tris propane, pH 7, 60% v/v tacsimate, cryoprotection: 4:1 reservoir:glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 298K |